Chemical Synthesis and Biological Activity of The Gelatinase Biosynthesis-Activating Pheromone of Enterococcus faecalis and Its Analogs

Jiro NAKAYAMA; Yong CAO; Takaaki HORII; Shohei SAKUDA; Hiromichi NAGASAWA

doi:10.1271/bbb.65.2322

Organic Chemistry

Chemical Synthesis and Biological Activity of The Gelatinase Biosynthesis-Activating Pheromone of Enterococcus faecalis and Its Analogs

Jiro NAKAYAMA, Yong CAO, Takaaki HORII, Shohei SAKUDA, Hiromichi NAGASAWA

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Keywords: gelatinase biosynthesis-activating pheromone, Enterococcus faecalis, peptide lactone, peptide pheromone, quorum sensing

JOURNAL FREE ACCESS

2001 Volume 65 Issue 10 Pages 2322-2325

DOI https://doi.org/10.1271/bbb.65.2322

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Abstract

An 11-residue peptide lactone, termed the gelatinase biosynthesis-activating pheromone (GBAP), triggers the production of the pathogenicity-related extracellular proteases, gelatinase and serine protease, in Enterococcus faecalis. In this study, we synthesized GBAP and its analogs and examined their gelatinase biosynthesis-inducing activity. This study on the structure-activity relationship shows that a lactone ring was indispensable for the activity.

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